Sites of in vivo phosphorylation of histone H5.

@article{Sung1978SitesOI,
  title={Sites of in vivo phosphorylation of histone H5.},
  author={M T Sung and Elizabeth F. Freedlender},
  journal={Biochemistry},
  year={1978},
  volume={17 10},
  pages={1884-90}
}
Previous studies have suggested that the phosphorylation and dephosphorylation of histone H5 play an important role in controlling the condensation of avian erythrocyte chromatin. The present work locates in the polypeptide chain the major sites at which H5 is phosphorylated in vivo. The majority of the radioactivity in 32P-labeled H5 is clustered in two regions of the molecule. Nearly 50% of the 32P is found in the amino-terminal N-bromosuccinimide (NBS) peptide (residues 1-28); the remainder… CONTINUE READING